KEGG   ENZYME: 3.4.21.43
Entry
EC 3.4.21.43                Enzyme                                 
Name
classical-complement-pathway C3/C5 convertase;
C3 convertase;
C_overbar_42_;
C4b,2a;
C5 convertase;
C_overbar_423_;
C4b,2a,3b;
C42;
C423;
complement C.hivin.4.hivin2;
complement C3 convertase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
Reaction(IUBMB)
Selective cleavage of Arg!Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg! bond in complement component C5 alpha-chain to form C5a and C5b
Comment
A complex of complement fragments C4b, C2a and C2b. C2a contains the active site, C2b the site for C4b binding. C2a and C2b are formed by cleavage of proenzyme C2 by complement subcomponent C_overbar_1s_. Cleavage of C5 requires complement fragment C3b which binds C5 and renders it susceptible to cleavage by the C4b,2a complex. Includes former EC 3.4.21.44. Complement component C2a is in peptidase family S1 (trypsin family)
History
EC 3.4.21.43 created 1981 (EC 3.4.21.44 created 1981, incorporated 1984)
Orthology
K01332  complement component 2
Genes
HSA717(C2)
PTR100608992(C2)
PPS103783827(C2)
GGO101145799(C2)
PON100173033(C2)
NLE100606928(C2)
MCC106997899(C2)
MCF102137096(C2)
CSAB103221735(C2)
CATY105583240(C2)
TGE112622243(C2)
RRO104678122(C2)
RBB108520263(C2)
TFN117086977(C2)
CJC103792363(C2)
SBQ104650316(C2)
CSYR103271297(C2)
MMUR105858160(C2)
OGA100948920(C2)
MMU12263(C2)
MCAL110312387(C2)
MPAH110336126(C2)
RNO24231(C2)
MCOC116075350(C2)
MUN110560138(C2)
CGE100759069(C2)
PLEU114705865(C2)
NGI103724419(C2)
HGL101723809(C2)
CPOC100716184(C2)
CCAN109689592(C2)
DORD105999865(C2)
DSP122111495(C2)
NCAR124989526
OCU100355553(C2)
OPI101519169(C2)
TUP102480144(C2)
CFA474853(C2)
VVP112913623(C2)
VLG121500782(C2)
AML100474163(C2)
UMR103682287(C2)
UAH113243740(C2)
UAR123790974(C2)
ELK111152312
LLV125101523
MPUF101692540(C2)
ORO101377842(C2)
EJU114222260(C2)
ZCA113927723(C2)
MLX118027318(C2)
FCA101092434(C2)
PYU121022335(C2)
PBG122478264(C2)
PTG102969252(C2)
PPAD109260505(C2)
AJU106983482(C2)
HHV120221933(C2)
BTA515440(C2)
BOM102269155(C2)
BIU109576932(C2)
BBUB102406076(C2)
CHX102176085(C2)
OAS101115321(C2)
ODA120870574(C2)
CCAD122429826(C2)
SSC448981(C2)
CFR102518989(C2)
CDK105087440(C2)
VPC102528144(C2)
BACU103018276(C2)
LVE103071578(C2)
OOR101281566(C2)
DLE111170704(C2)
PCAD102992128(C2)
PSIU116762860(C2)
ECB100059162(C2)
EPZ103563291(C2)
EAI106831000(C2)
MYB102263362(C2)
MYD102766284(C2)
MMYO118679566(C2)
MLF102434614 102435622(C2)
MNA107538982(C2)
SHON118979560(C2)
AJM119053694(C2)
PDIC114494189(C2)
PHAS123810445(C2)
MMF118621434(C2)
RFQ117020467(C2)
PALE102889530(C2)
PGIG120618902(C2)
PVP105305295(C2)
RAY107498438(C2)
MJV108393991(C2)
TOD119252228(C2)
LAV100668309(C2)
TMU101350027
MDO100025443(C2)
GAS123243666(C2)
SHR105750443(CFB)
PCW110199442(C2)
OAA100089242
GGA419574(C2)
PCOC116230112(C2)
MGP104914277
CJO107323905
NMEL110387356
ACHC115338421(CFB)
ASN102381270(CFB)
AMJ102574290(C2)
CPIC101947880
CABI116829917
ACS100556178(c2)
PVT110088698(C2)
SUND121922133(C2)
PBI103049015
PMUR107295035
ZVI118080127
GJA107105482
XLA734198(c2.L)
XTR100491079(c2)
NPR108786508
RTEM120913253
BBUF120977489
BGAR122946772
DRE563828(si:ch1073-280e3.1)
SRX107720441
SANH107662575
SGH107567682
CCAR109055343
CAUA113115417
IPU100862743(si:ch1073-280e3.1)
PHYP113539139
SMEO124394571(si:ch1073-280e3.1)
TFD113643603(si:ch1073-280e3.1)
AMEX103046310
EEE113574701
TRU101064033
TNGGSTEN00026804G001
LCO104930441
NCC104962863
CGOB115017381
ELY117259163(si:ch1073-280e3.1)
PLEP121942912(si:ch1073-280e3.1)
SLUC116039027(si:ch1073-280e3.1)
ECRA117942570(si:ch1073-280e3.1)
PFLV114549828
GAT120816446(si:ch1073-280e3.1)
PPUG119223014(si:ch1073-280e3.1)
MSAM119882756(si:ch1073-280e3.1)
CUD121523692(si:ch1073-280e3.1)
MZE101480328
ONL100697699
OAU116323697(si:ch1073-280e3.1)
OLA101167637
OML112136450(si:ch1073-280e3.1)
XMA102229083
XCO114161640
XHE116737354
PRET103474842
PFOR103154630
PLAI106965101
PMEI106914174
GAF122832266(si:ch1073-280e3.1)
CVG107102499
CTUL119775419(si:ch1073-280e3.1)
GMU124883852(si:ch1073-280e3.1)
NFU107397014
KMR108244431(si:ch1073-280e3.1)
ALIM106530408
NWH119411148(si:ch1073-280e3.1)
AOCE111574507
POV109642964
SSEN122772936(si:ch1073-280e3.1)
HHIP117772604(si:ch1073-280e3.1)
LCF108890635
XGL120792530(si:ch1073-280e3.1)
BPEC110162865
SASA106580826
OTW112265208(si:ch1073-280e3.1)
OMY100135805(si:ch1073-280e3.1)
OGO123992917(si:ch1073-280e3.1)
ONE115136963
SALP111982534
SNH120018329(si:ch1073-280e3.1)
ELS105011227
SFM108928780
PKI111854971
AANG118209021(si:ch1073-280e3.1)
LOC102694189 107079953
PSPA121304122
ARUT117433872(si:ch1073-280e3.1) 117971245
RTP109921429
BFO118420754
CIN497243(bf-1) 619241(bf-2)
SPU754422 756500 756883
APLC110983861
SKO100368814
PCHN125029930
PTEP107450490
LAK106177660 106178727
NVE5501707 5502106 5515331
EPA110235255 110235277 110235590 110242877 110244509 110253640
ATEN116298611 116308431 116308433
ADF107349284 107355215
AMIL114946777 114954057 114977272
PDAM113668202 113675686
SPIS111328750 111343603 111345231
 » show all
Reference
1
  Authors
Kerr, M.A.
  Title
The second component of human complement.
  Journal
Method Enzymol 80:54-64 (1981)
Reference
2  [PMID:3052276]
  Authors
Muller-Eberhard HJ.
  Title
Molecular organization and function of the complement system.
  Journal
Annu Rev Biochem 57:321-47 (1988)
DOI:10.1146/annurev.bi.57.070188.001541
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.43
IUBMB Enzyme Nomenclature: 3.4.21.43
ExPASy - ENZYME nomenclature database: 3.4.21.43
BRENDA, the Enzyme Database: 3.4.21.43
CAS: 56626-15-4

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